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Database: UniProt
Entry: G3TQ81_LOXAF
LinkDB: G3TQ81_LOXAF
Original site: G3TQ81_LOXAF 
ID   G3TQ81_LOXAF            Unreviewed;       381 AA.
AC   G3TQ81;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Protein kinase cAMP-dependent type I regulatory subunit beta {ECO:0000313|Ensembl:ENSLAFP00000017679.2};
GN   Name=PRKAR1B {ECO:0000313|Ensembl:ENSLAFP00000017679.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017679.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000017679.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017679.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000017679.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017679.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   AlphaFoldDB; G3TQ81; -.
DR   STRING; 9785.ENSLAFP00000017679; -.
DR   Ensembl; ENSLAFT00000022101.2; ENSLAFP00000017679.2; ENSLAFG00000022863.2.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000157513; -.
DR   InParanoid; G3TQ81; -.
DR   OMA; QILAWQK; -.
DR   TreeFam; TF314920; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12102; DD_RIbeta_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR042818; RIbeta_DD.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-BETA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   3: Inferred from homology;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW   1}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          137..252
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          255..376
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          68..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         202
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         211
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         326
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         335
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ   SEQUENCE   381 AA;  43199 MW;  1ACBDD3595E257F8 CRC64;
     MASPSPWLSE EDESLKGCEL YVHKHSIQQV LKECIVHLCV AKPDRPMKFL REYFEKLEKE
     ENKQILAWQK SSSQSDSHEE EISPMPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK
     DYKTMTALAK AISKNVLFAH LDDNERSDIF DAMFPVTHIA GEIVIQQGDE GDNFYVIDQG
     EVDVYVNGEW VTSISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL
     RKRKMYDEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGAPGD DFYIITEGTA
     SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG
     PCSEILKRNI QRYNSFISLT V
//
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